Interaction of calcium-independent latrotoxin receptor with intracellular adapter protein TRIP8b.
Interaction of calcium-independent latrotoxin receptor with intracellular adapter protein TRIP8b.
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钙非依赖性河豚毒素受体与细胞内接头蛋白 TRIP8b 的相互作用。
DOI：
10.1134/s1607672907030155
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发表时间：
2007
期刊：
影响因子：
--
通讯作者：
Petrenko,AG
中科院分区：
文献类型：
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作者：
Popova,NV;Plotnikov,A;Deev,IE;Petrenko,AG
Popova等人。洗脱后的蛋白用SDS-PAGE分离，转移到硝酸纤维素膜上，与兔抗TRIP8b C末端抗体孵育。图1显示，从对照树脂收集的洗脱液中不存在TRIP8b，而从吸附了GST-CT2的树脂收集的洗脱液中存在TRIP8b。TRIP8b的C-末端部分包含六个TPR基序，形成TPR结构域。TPR基序是由34个氨基酸残基组成的重复序列；它们存在于许多蛋白质中，参与蛋白质之间的相互作用[8]。这些重复序列经常一个接一个地定位，结果形成了由两个反平行的α-螺旋结合到一个短环上的空间结构[9]。TRIP8b的N-末端部分与其他已知蛋白质没有同源性；此外，它还经历了选择性剪接[10]。我们比较了不同生物的TRIP8b的氨基酸序列。我们使用的是TRIP8b的N-末端部分，它位于TPR基序之前，与其他蛋白质没有同源性，因此只能用于检测TRIP8b。图2显示了它们的系统发育
POPOVA et al. proteins eluted were separated by SDS-PAGE and transferred onto a nitrocellulose membrane which was incubated with rabbit antibodies to the C-terminal part of TRIP8b. Figure 1 shows that TRIP8b was absent in the eluate collected from the control resin and present in the eluate collected from the resin with adsorbed GST-CT2.The C-terminal part of TRIP8b contains six TPR motifs which form the TPR domain. TPR motifs are repeats consisting of 34 amino acid residues; they are present in many proteins and involved in protein–protein interactions [8]. These repeats are frequently located one after another and, as a result, form spatial structure which consists of two antiparallel α-helices bound to a short loop [9]. The TRIP8b N-terminal part has no homology with other known proteins; in addition, it undergoes alternative splicing [10]. We compared the amino acid sequences of TRIP8b from various organisms. We used the N-terminal part of TRIP8b, which is located before the TPR motifs, has no homology with other proteins, and, hence, can be used to detect only TRIP8b. Figure 2 shows the phylogenetic